Our research activities fall within 3 main areas, which all relate to the study of the kinetics and thermodynamics of protein conformational changes, namely membrane protein folding, protein-detergent interactions and protein fibrillation. These areas are linked by a keen interest in understanding the mechanistic and thermodynamic behaviour of proteins in different circumstances by quantifying the strength of internal side-chain interactions as well as contacts with solvent molecules, whether it be detergents, denaturants, stabilizing salts and osmolytes or lipids. Ultimately we hope this will lead to a greater manipulative ability vis-a-vis processes of both basic, pharmaceutical and industrial relevance. The general approach is to use available spectroscopic techniques (fluorescence, CD, stopped-flow, FTIR, NMR and dynamic and static light scattering) to generate data which can be analyzed in a quantitative manner to develop models and mechanisms for conformational changes at the molecular level.
2019.10.24 | iNano
New Danish collaboration between companies and researchers aims to develop a completely new method of recycling a specific type of plastic, which would otherwise end up on incineration plants for energy recovery or at the landfill. The technology is expected to help reduce oil consumption and CO2 emissions.
2019.10.11 | iNano
Partial unfolding of proteins can be a big problem in industry, as it may affect the stability of products. So how does an empty space or cavity in its hydrophobic core destabilize a protein? And would such a cavity in fact be empty? These are some of the questions researchers from Aarhus University answer in a new study.
2019.10.09 | iNano
PhD student in Associate Professor Henrik Birkedals research group receives poster prize at the European Synchrotron Radiation Facility
